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Structure of the pressure-assisted cold denatured state of ubiquitin.

Authors
Type
Published Article
Journal
Biochemical and Biophysical Research Communications
0006-291X
Publication Date
Volume
238
Issue
2
Pages
289–291
Identifiers
PMID: 9299496
Source
Medline

Abstract

The pressure-assisted cold denatured state of ubiquitin in aqueous solution was investigated by high resolution NMR. Hydrogen exchange kinetics were measured for backbone amide protons in the cold denatured protein to determine its structure. In contrast to cold denatured ribonuclease A and lysozyme, cold denatured ubiquitin shows little persistent secondary structure. The behavior of ubiquitin supports the idea of a relationship between the residual structure of pressure-assisted cold-denatured states and the structure of early folding intermediates provided they exist.

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